CPSF5_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CPSF5_RAT
• UniProt AC: Q4KM65
• Protein Name: Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000250|UniProtKB:O43809}
• Gene Name: Nudt21 {ECO:0000312|RGD:1305766}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 227
• Subcellular Localization: Nucleus . Cytoplasm . Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm). In punctate subnuclear structures localized adjacent to nu
• Protein Description: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7. Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function. Binds to chromatin. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides..
• Protein Sequence: MSVVPPNRSQTGWPRGVNQFGNKYIQQTKPLTLERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDKIGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNPGEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNFEPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKLVAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYN

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSVVPPNRS ------CCCCCCCCC	31.64	-
15	Methylation	RSQTGWPRGVNQFGN CCCCCCCCCCHHHCC	56.00	-
23	Acetylation	GVNQFGNKYIQQTKP CCHHHCCCCCCCCCC	44.07	25786129
29	Acetylation	NKYIQQTKPLTLERT CCCCCCCCCEEEEEE	33.42	26302492
40	Phosphorylation	LERTINLYPLTNYTF EEEEEEEEECCCCCC	7.54	-
56	Acetylation	TKEPLYEKDSSVAAR CCCCCCCCCHHHHHH	49.72	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CPSF5_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CPSF5_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CPSF5_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of CPSF5_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.